Kallikrein-related peptidases are activators of the CC chemokine CCL14.

Abstract

Chemokine CCL14 is inactive in its proform. Here, we show that inflammation- and cancer-associated kallikrein-related peptidases KLK5 and KLK8 remove the N-terminal eight amino acids from the proform thereby converting CCL14 to its active state. Activity of the chemokine is demonstrated by migration of myeloid cells expressing relevant receptors.

• Authors: Mario Grünberg, Dagmar Quandt, Holger Cynis, Hans-Ulrich Demuth, Andrea Kindermann, Viktor Magdolen, Wolf-Georg Forssmann, Barbara Seliger, Hans-Jürgen Mägert
• Journal: European journal of immunology (Eur J Immunol) Vol. 48 Issue 9 Pg. 1592-1594 (09 2018) ISSN: 1521-4141 [Electronic] Germany
• PMID: 30028015 (Publication Type: Letter, Research Support, Non-U.S. Gov't)
• Copyright: © 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Chemical References

• CCL14 protein, human
• CCL15 protein, human
• CX3CL1 protein, human
• CXCL12 protein, human
• CXCL8 protein, human
• Chemokine CX3CL1
• Chemokine CXCL12
• Chemokines
• Chemokines, CC
• Interleukin-8
• Macrophage Inflammatory Proteins
• Reactive Oxygen Species
• KLK5 protein, human
• KLK8 protein, human
• Kallikreins

Topics

• Asthma (pathology)
• Atherosclerosis (pathology)
• Cell Line, Tumor
• Chemokine CX3CL1 (metabolism)
• Chemokine CXCL12 (metabolism)
• Chemokines (metabolism)
• Chemokines, CC (metabolism)
• Crohn Disease (pathology)
• Enzyme Activation
• Humans
• Interleukin-8 (metabolism)
• Kallikreins (metabolism)
• Leukemia (pathology)
• Macrophage Inflammatory Proteins (metabolism)
• Pancreatitis (pathology)
• Reactive Oxygen Species (metabolism)